Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor

Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor

We report a highly reproducible method to crystallize the RNA-dependent RNA polymerase (RdRp) domain of dengue virus serotype 3 (DENV-3), allowing structure refinement to a 1.79-Å resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal struct...

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Bibliographic Details
Main Authors: Yap, Lijian, Lescar, Julien, Noble, Christian G., Lim, Siew Pheng, Chen, Yen-Liang, Liew, Chong Wai, Shi, Pei-Yong
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2015
Subjects:
DRNTU::Science::Biological sciences::Microbiology::Virology
Online Access:https://hdl.handle.net/10356/103700
http://hdl.handle.net/10220/25795
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Institution: Nanyang Technological University
Language: English
Description
Summary:We report a highly reproducible method to crystallize the RNA-dependent RNA polymerase (RdRp) domain of dengue virus serotype 3 (DENV-3), allowing structure refinement to a 1.79-Å resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal structure at a 2.1-Å resolution. The inhibitor binds to the RdRp as a dimer and causes conformational changes in the protein. The improved crystallization conditions and new structural information should accelerate structure-based drug discovery.

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